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HAF007). Specific bands were detected for BACE-1 at approximately 60 and 70 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox" target="_blank">
ES004) by Recombinant Human BACE-1 (10 µg/mL, Catalog # 931-AS) or Recombinant Mouse BACE-1 (10 µg/mL, Catalog # 2976-AS) is measured after preincubation with increasing concentrations of Mouse Anti-Human/Mouse BACE-1 Ectodomain Monoclonal Antibody (Catalog # MAB9311). The ND50 is typically 10 µg/mL.a" class="big_lightbox" target="_blank">
BACE1 is a protease responsible for the proteolytic processing of the amyloid precursor protein (APP). Amyloid beta peptide is the major constituent of amyloid plaques in the brains of individuals afflicted with Alzheimers disease. This peptide is generated from the beta-amyloid precursor protein (beta APP) in a two-step process. The first step involves cleavage of the extracellular, amino-terminal domain of beta APP. Protein cleavage is performed by an aspartyl protease termed beta-secretase (BACE), of which there are two isoforms, BACE1 and 2. This enzyme is synthesized as a propeptide that must be modified to the mature and active form by the prohormone convertase furin. Beta APP cleavage by the mature form of BACE results in the cellular secretion of a segment of beta APP and a membrane-bound remnant. This remnant is then processed by another protease termed gamma-secretase. Gamma-secretase cleaves an intra-membrane site in the carboxyl-terminal domain of beta APP, thus generating the amyloid beta peptide.